Enzyme activities in type I and II muscle fibres of human skeletal muscle in relation to age and torque development

Borges, O.; Essén‐Gustavsson, Birgitta

doi:10.1111/j.1748-1716.1989.tb08626.x

Cited by 63 publications

(35 citation statements)

References 24 publications

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“…This finding supports previous data that observed age-related decreases in CK in human skeletal muscle [141]. In contrast, a number of previous studies have observed no age-related change in CK activity in weightbearing muscles such as vastus lateralis [17], gastrocnemius [32], or ankle dorsi flexors measured using phosphorous magnetic resonance spectroscopy [93]. Of interest in the Lanza and others [93] study is that both the rate of PCr hydrolysis during the first 6 s of a 60-s maximal isometric contraction of the ankle dorsi flexors and the overall and peak glycolytic rate were significantly faster in young (20-35 years) versus older (65-80 years) men.…”

Section: Efficiency Of Metabolic Pathwayssupporting

confidence: 91%

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Anaerobic performance in masters athletes

Reaburn

Dascombe²

2008

Eur Rev Aging Phys Act

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With increasing age, it appears that masters athletes competing in anaerobic events (10-100 s) decline linearly in performance until 70 years of age, after which the rate of decline appears to accelerate. This decline in performance appears strongly related to a decreased anaerobic work capacity, which has been observed in both sedentary and well-trained older individuals. Previously, a number of factors have been suggested to influence anaerobic work capacity including gender, muscle mass, muscle fiber type, muscle fiber size, muscle architecture and strength, substrate availability, efficiency of metabolic pathways, accumulation of reaction products, aerobic energy contribution, heredity, and physical training. The effects of sedentary aging on these factors have been widely discussed within literature. Less data are available on the changes in these factors in masters athletes who have continued to train at high intensities with the aim of participating in competition. The available research has reported that these masters athletes still demonstrate agerelated changes in these factors. Specifically, it appears that morphological (decreased muscle mass, type II muscle fiber atrophy), muscle contractile property (decreased rate of force development), and biochemical changes (changes in enzyme activity, decreased lactate production) may explain the decreased anaerobic performance in masters athletes.However, the reduction in anaerobic work capacity and subsequent performance may largely be the result of physiological changes that are an inevitable result of the aging process, although their effects may be minimized by continuing specific high-intensity resistance or sprint training.

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Section: Efficiency Of Metabolic Pathwayssupporting

confidence: 91%

“…In younger individuals, it has been observed that, relative to similar-aged men, women display: [17] The limited data available suggest that both men and women can both increase their anaerobic capacities signif- icantly in response to anaerobic training [98,155].…”

Section: Gendermentioning

confidence: 99%

Anaerobic performance in masters athletes

Reaburn

Dascombe²

2008

Eur Rev Aging Phys Act

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“…The absolute values for AK activity of our adult subjects is consistent with other reports (39,40), and to our knowledge, The effect of age on muscle OGDH and CPT activity. *Significantly different (p Ͻ 0.04) OGDH activity between children (n ϭ 19) and adults (n ϭ 12).…”

Section: Discussionsupporting

confidence: 80%

Anaerobic and Aerobic Enzyme Activities in Human Skeletal Muscle from Children and Adults

et al. 2005

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Literature has shown that children have lower anaerobic capacity and oxidize more lipids during aerobic activity compared with adults. The purpose of the present study was to examine the effects of age on the activity of marker enzymes for anaerobic and aerobic metabolism in human skeletal muscle from relatively sedentary children and adults. The m. obliquus internus abdominis was analyzed for anaerobic [creatine kinase, adenylate kinase, and lactate dehydrogenase (LDH)] and aerobic (carnitine palmitoyltransferase and 2-oxoglutarate dehydrogenase) enzyme activities in 32 male individuals. The subjects were divided into two groups: children (3-11 y; n ϭ 20) and adults (29 -54 y; n ϭ 12). LDH activity was higher in adults (118.2 Ϯ 20.1) compared with children (27.8 Ϯ 10.1) mol · min Ϫ1 · g Ϫ1 wet weight (p Ͻ 0.0002). Creatine kinase activity was 28% (p Ͻ 0.0003) lower in children than in adults, and adenylate kinase activity was 20% (p Ͻ 0.006) lower in children than in adults. In addition, we found higher 2-oxoglutarate dehydrogenase activity in adults compared with children (p Ͻ 0.04), with no effect of age on carnitine palmitoyltransferase activity (NS). When samples were expressed relative to protein content, only LDH activity remained significantly lower in children compared with adults (p Ͻ 0.0001). In conclusion, the lower LDH activity observed in children compared with adults may partially explain decreased anaerobic and lactate generation capacity of the children studied. However, the mechanisms for the relatively deficient anaerobic enzyme activities of children are not clear. The functional characteristics of human skeletal muscle are partially dependent on fiber type; however, modifications to the nature and the capacity of the energy-delivering metabolic pathways can occur independent of fiber type. It is widely known that metabolic enzymes in skeletal muscle have the ability to respond to physiologic stimuli such as exercise (1-4), as well as pathologic processes such as muscular dystrophy, acute respiratory failure, mitochondrial myopathy, denervation, and inactivity (5-9). Although there is some controversy regarding fiber type differences between children and adults (10 -13), there are only minor increases in the proportion of type II fibers with age (10 -12), with no difference in ultrastructure (13). Moreover, there is still disagreement over the effect of age on the enzymatic capacity of skeletal muscle, particularly during the maturation from the pediatric to the adult age group.It has been reported that phosphofructokinase (PFK) was 3-fold lower in the skeletal muscle of children (11-13 y) compared with adults (24 -52 y); however, succinate dehydrogenase activity was not significantly altered by age (11,14). Other studies that have examined anaerobic enzyme activity in children have reported lower glycolytic [PFK, lactate dehydrogenase (LDH)] and higher aerobic (succinate dehydrogenase, fumarase) enzyme activities in children compared with younger adults (14,15). In contrast, one report demon...

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“…CK activity has also been reported to be significantly higher in fast glycolytic than in slow oxidative muscle fibers (59), although others find no difference (9). This discrepancy might be explained by our observation that CK activities in rat skeletal muscles change with age in soleus muscle (Table 2).…”

Section: Discussioncontrasting

confidence: 55%

PGC-1α and PGC-1β have both similar and distinct effects on myofiber switching toward an oxidative phenotype

Mortensen¹,

Frandsen²,

Schjerling³

et al. 2006

American Journal of Physiology-Endocrinology and Metabolism

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Mortensen, Ole Hartvig, Lis Frandsen, Peter Schjerling, Erica Nishimura, and Niels Grunnet. PGC-1␣ and PGC-1␤ have both similar and distinct effects on myofiber switching toward an oxidative phenotype. Am J Physiol Endocrinol Metab 291: E807-E816, 2006. First published May 23, 2006 doi:10.1152/ajpendo.00591.2005.-Peroxisome proliferator-activated receptor-␥ coactivator-1␣ and -1␤ (PGC-1␣ and PGC-1␤) were overexpressed by adenovirus-mediated gene transfer in cultures of primary rat skeletal muscle cells derived from neonatal myoblasts. Effects on muscle fiber type transition and metabolism were studied from days 5 to 22 of culture. PGC-1␣ and PGC-1␤ overexpression caused a three-to fourfold increase in mRNA level, a doubling of enzymatic activity of citrate synthase, a slight increase in short-chain acyl-CoA dehydrogenase mRNA, a doubling of the mRNA level, and a 30 -50% increase in enzymatic activity of glyceraldehyde-3-phosphate dehydrogenase. Lactate dehydrogenase or creatine kinase activity was unchanged. PGC-1␣ enhanced glycogen buildup twofold at 5 or 25 mM glucose, whereas PGC-1␤ caused a decrease. Both PGC-1␣ and PGC-1␤ overexpression caused a faster maturation of myotubes, as seen by mRNA downregulation of the immature embryonal and perinatal myosin heavy-chain (MHC) isoforms. PGC-1␣ or PGC-1␤ overexpression enhanced mRNA of the slow oxidative-associated MHC isoform MHCIb and downregulated mRNA levels of the fast glycolytic-associated MHC isoforms MHCIIX and MHCIIB. Only PGC-1␤ overexpression caused an increase in mRNA of the intermediary fast oxidative-associated MHC isoform MHCIIA. PGC-1␣ or PGC-1␤ overexpression upregulated GLUT4 mRNA and downregulated myocyte enhancer factor 2C transcription factor mRNA; only PGC-1␣ overexpression caused an increase in the mRNA expression of TRB3, a negative regulator of insulin signaling. These results show that both PGC-1␣ and PGC-1␤ are involved in the regulation of skeletal muscle fiber transition and metabolism and that they have both overlapping and differing effects. skeletal muscle cell culture; peroxisome proliferator-activated receptor ␥ coactivator-1; myosin heavy chain; enzyme activities; glycogen THE BENEFICIAL EFFECT of exercise on various diseases is widely acknowledged (7), and exercise has proven particularly successful as a treatment for the metabolic syndrome, including type 2 diabetes (48); however, the exact molecular pathway responsible for the effect is largely unknown. Recently, genes involved in oxidative phosphorylation in skeletal muscle were found to be downregulated in patients with type 2 diabetes (37, 43), and speculations about type 2 diabetes being caused by mitochondrial dysfunction, primarily in the type I skeletal muscle fibers, have surfaced (13,31,51). Regular exercise has been shown to induce changes in both skeletal muscle metabolism and muscle fiber type over time, most notably an increase in mitochondrial content and oxidative metabolism as well as a shift toward a more slow oxidative fiber type (8,44).

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Enzyme activities in type I and II muscle fibres of human skeletal muscle in relation to age and torque development

Cited by 63 publications

References 24 publications

Anaerobic performance in masters athletes

Anaerobic performance in masters athletes

Anaerobic and Aerobic Enzyme Activities in Human Skeletal Muscle from Children and Adults

PGC-1α and PGC-1β have both similar and distinct effects on myofiber switching toward an oxidative phenotype

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